Crystal structure of a novel non-Pfam protein PF2046 solved using low resolution B-factor sharpening and multi-crystal averaging methods.
10.1007/s13238-010-0045-7
- Author:
Jing SU
1
;
Yang LI
;
Neil SHAW
;
Weihong ZHOU
;
Min ZHANG
;
Hao XU
;
Bi-Cheng WANG
;
Zhi-Jie LIU
Author Information
1. National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
- Publication Type:Journal Article
- MeSH:
Bacterial Proteins;
chemistry;
Crystallography, X-Ray;
Models, Molecular;
Protein Conformation;
Pyrococcus furiosus;
chemistry;
Solubility
- From:
Protein & Cell
2010;1(5):453-458
- CountryChina
- Language:English
-
Abstract:
Sometimes crystals cannot diffract X-rays beyond 3.0 Å resolution due to the intrinsic flexibility associated with the protein. Low resolution diffraction data not only pose a challenge to structure determination, but also hamper interpretation of mechanistic details. Crystals of a 25.6 kDa non-Pfam, hypothetical protein, PF2046, diffracted X-rays to 3.38 Å resolution. A combination of Se-Met derived heavy atom positions with multiple cycles of B-factor sharpening, multi-crystal averaging, restrained refinement followed by manual inspection of electron density and model building resulted in a final model with a R value of 23.5 (R(free)= 24.7). The asymmetric unit was large and consisted of six molecules arranged as a homodimer of trimers. Analysis of the structure revealed the presence of a RNA binding domain suggesting a role for PF2046 in the processing of nucleic acids.
